Physical-mathematical model to predict the kinetic coagulation process by clotting activity of bacterial endopeptidases
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A physical-mathematical model was used to evaluate the capability of an enzymatic pool
of Bacillus sp. P7 (isolated from Piaractus mesopotamicus) to promote the bovine casein
micelles coagulation. Experiments were designed to assess the effects of temperature, pH,
and enzyme activity/mass of substrate ratio on the kinetic parameters of the coagulation
process and the microstructure of the obtained clots. Descriptive and predictive equations
indicate that the temperature and the pH modified these parameters significantly. In
optimal conditions, the clot’s mean pore size was 3.6 times smaller using chymosin. On
the other hand, rheological measurements evidence a moderate elasticity of clot, which
indicates the usefulness of P7 protease preparation as a clotting agent in spreadable or
soft cheese manufacture. Also, the hydrolysis products, which are in the whey after casein
micelles coagulation, demonstrated antioxidant activities. Equations to model and predict
the process kinetics were combined with rheological and microstructure analyses of the
obtained clots, and whey bioactivities were evaluated. Nevertheless, the use of P7PP
requires further investigation concerning the stability of the enzyme preparation during
storage, its performance, and how these variables could be related to the proposed models.
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